Protein Metabolism ¾ body solids-proteins

Blood Aa

 blood 35-65 mg/dl->average 2 mg/dl for each of 20 aa

 ionized state, 2 to 3 mEq of negative ions in blood

Fate of Aa Absorbed from GIT

 after meal, aa concentration in blood rises only a few mg per deciliter

 protein digestion and absorption - 2 to 3 h-> small quantities absorbed at a time
 excess aa absorbed within 5-10 min by cells, especially liver

R' Renal Threshold for Aa

 In kidneys, aa can be actively reabsorbed through proximal tubular epithelium

 removes them from glomerular filtrate and returns to blood
 there is an upper limit to rate at which each type of aa can be transported
 concentration of aa too high in plasma and glomerular filtrate, excess cannot be reabsorbed

Storage of Aa as Proteins in the Cells

 concentration of aa inside cells remains low

 stored mainly in form of actual proteins
 decomposed again into aa under influence of intracellular lysosomal digestive enzymes;
 exceptions-proteins in chromosomes of nucleus collagen, muscle proteins;
 liver-store large quantities of rapidly exchangeable proteins;
 true to a lesser extent of kidneys and intestinal mucosa

Release of Aa from Cells as a Means of Regulating Plasma Aa Concentration.

 hormones -alter balance between tissue proteins and circulating aa

 growth hormone and insulin increase formation of tissue proteins
 adrenocortical glucocorticoid hormones increase the concentration of plasma aa

Reversible Equilibrium Between Proteins in Different Parts of Body

 proteins in liver (less extent, in other tissues) synthesized rapidly from plasma aa
 many proteins can be degraded and returned to plasma almost as rapidly
 constant equilibrium between plasma aa and labile proteins in virtually all cells of body
 particular tissue requires proteins synthesize new proteins from aa of blood;
 blood aa are replenished by degradation of proteins from other cells especially liver
 Each particular cell has - limit - aa still in circulation->fat or glycogen

Functional Roles of the Plasma Proteins

 albumin - provide colloid osmotic pressure - prevents plasma loss from capillaries
 globulins - enzymatic functions in plasma, body’s immunity
 Fibrinogen-polymerizes into long fibrin threads during blood coagulation
Formation of the Plasma Proteins

 all albumin and fibrinogen, 50-80% globulins, formed in liver, rest-lymphoid tissues
 gamma globulins-constitute antibodies used in immune system
 rate of plasma protein formation by liver 30 g/day
 person with severe renal disease loses 20 gs of plasma protein in urine each day
 cirrhosis of liver, fibrous tissue develop among liver parenchymal cells-> -- plasma proteins
 decreased plasma colloid osmotic pressure, generalized edema

Plasma Proteins as a Source of Aa for the Tissues.

 plasma proteins-imbibed by tissue macrophages through pinocytosis;

 in these cells, split into aa that are transported back into blood and used throughout body

Reversible Equilibrium Between the Plasma Proteins and the Tissue Proteins.

 equilibrium, among plasma proteins, aa of plasma, tissue proteins

 400 gs of body protein are synthesized and degraded each day
 Even during starvation -ratio of total tissue proteins to total plasma proteins-33:1
 acute wholebody protein deficiency-intravenous transfusion of plasma protein

Essential and Nonessential Aa

 Synthesis of nonessential aa depends on formation of appropriate a-keto acids, precursors

 pyruvic acid, keto acid precursor of alanine
 Glutamine is present in tissues in large quantities, amino radical storehouse
 amino radicals can be transferred from asparagine, glutamic acid, aspartic acid
 Transamination is promoted by aminotransferases, derivatives of pyridoxine

Use of Proteins for Energy -occurs almost entirely in liver

Deamination

Urea Formation by the Liver.

 ammonia released in deamination of aa is removed from blood by conversion into urea;

 2 NH3 + CO2-> H2N—CO—NH2 + H2O
 all urea formed in human body is synthesized in liver

Oxidation of Deaminated Aa

 keto acids ->oxidized to release energy for metabolic purposes

  keto acid - changed into chemical substance that can enter citric acid cycle,
 degraded by cycle and used for energy in same manner as (acetyl-CoA)
 (ATP) formed for each g of protein that is oxidized is slightly less than of glucose

Gluconeogenesis and Ketogenesis.

 Certain deaminated aa-similar to substrates used by liver cells, synthesize glucose/fatty acids
 deaminated alanine=pyruvic acid-> glucose/glycogen/acetyl-CoA polymerized into fatty acids
 2 acetyl-CoA -> acetoacetic acid= ketone body
 18 have chemical structures that allow to be converted into glucose, 19 into fatty acids

Degradation of Proteins

 eats no proteins-body proteins degraded into aa 20-30 gs/day, obligatory loss of proteins
 one must ingest a minimum of 20-30 gs; 60-75 gs is usually recommended
 If one particular type of essential aa is low in concentration, others become unusable
 cells synthesize either whole proteins or none at all
 unusable aa-deaminated and oxidized- partial protein or incomplete protein

Effect of Starvation on Protein Degradation.

 body uses almost entirely carbohydrates or fats for energy

 starvation-> carbohydrates run out->aa oxidized ->125 gs daily-cellular funct deteriorate

Growth Hormone Increases the Synthesis of Cellular Proteins.

 tissue proteins to increase

 increased transport of aa through cell membranes ++ DNA and RNA
 lack of insulin reduces protein synthesis to 0
 ++ transport of aa to cells, stimul protein synthesis+ increases availability of glucose to cells

Glucocorticoids Increase Breakdown of Most Tissue Proteins

 ++ liver proteins and plasma proteins

 ++ rate of breakdown of extrahepatic proteins-> aa available in body fluids
 allows the liver to synthesize hepatic cellular proteins and plasma proteins

Testosterone Increases Protein Deposition in Tissues. especially muscles (30 to 50% increase

muscles reached max, despite continued administration of testosterone, protein deposition ceases

Thyroxine

 ++ metabolism of all cells and-indirectly affects protein metabolism

 insufficient carbs and fats available, thyroxine causes rapid degradation of proteins
 adequate quantities + aa available in extracellular fluid, thyroxine ++ rate of protein synthesis